Plant phosphoinositides—complex networks controlling growth and adaptation

Heilmann, Mareike; Heilmann, Ingo

doi:10.1016/j.bbalip.2014.09.018

Cited by 75 publications

(70 citation statements)

References 130 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It is therefore possible that a massive pool of PI4P is present in endomembranes but not available to target lipid sensors to this compartment (i.e. ‘occupied’ PI4P pool) 49 . However, such occupied PI4P pool does not generate negative membrane charges, and is therefore not relevant for the generation of membrane electrostatic fields.…”

Section: Discussionmentioning

confidence: 99%

A PtdIns(4)P-driven electrostatic field controls cell membrane identity and signalling in plants

Simon¹,

Platre²,

et al. 2016

View full text Add to dashboard Cite

Many signaling proteins permanently or transiently localize to specific organelles for function. It is well established that certain lipids act as biochemical landmarks to specify compartment identity. However, they also influence membrane biophysical properties, which emerge as important features in specifying cellular territories. Such parameters include the membrane inner surface potential, which varies according to the lipid composition of each organelle. Here, we found that the plant plasma membrane (PM) and the cell plate of dividing cells have a unique electrostatic signature controlled by phosphatidylinositol-4-phosphate (PI4P). Our results further reveal that, contrarily to other eukaryotes, PI4P massively accumulates at the PM, establishing it as a critical hallmark of this membrane in plants. Membrane surface charges control the PM localization and function of the polar auxin transport regulator PINOID, as well as proteins from the BRI1 KINASE INHIBITOR1 (BKI1)/MEMBRANE ASSOCIATED KINASE REGULATORs (MAKRs) family, which are involved in brassinosteroid and receptor-like kinase signaling. We anticipate that this PI4P-driven physical membrane property will control the localization and function of many proteins involved in development, reproduction, immunity and nutrition.

show abstract

Section: Discussionmentioning

confidence: 99%

A PtdIns(4)P-driven electrostatic field controls cell membrane identity and signalling in plants

Simon¹,

Platre²,

et al. 2016

View full text Add to dashboard Cite

show abstract

“…In turn, genetic evidence indicates that PtdIns(3,5)P 2 might be produced at the tonoplast and late endosomes (Heilmann and Heilmann, 2015;Hirano et al, 2015;Novakova et al, 2014;Simon et al, 2014Simon et al, , 2016Vermeer et al, 2006Vermeer et al, , 2009. The cellular distribution of PtdIns5P in plants is unknown and neither PtdIns (3,4)P 2 nor PtdIns(3,4,5)P 3 have as yet been detected in plants (Heilmann, 2009;Munnik and Nielsen, 2011).…”

Section: Discussionmentioning

confidence: 99%

Phospholipid composition and a polybasic motif determine D6 PROTEIN KINASE polar association with the plasma membrane and tropic responses

et al. 2016

Self Cite

View full text Add to dashboard Cite

Polar transport of the phytohormone auxin through PIN-FORMED (PIN) auxin efflux carriers is essential for the spatiotemporal control of plant development. The Arabidopsis thaliana serine/threonine kinase D6 PROTEIN KINASE (D6PK) is polarly localized at the plasma membrane of many cells where it colocalizes with PINs and activates PIN-mediated auxin efflux. Here, we show that the association of D6PK with the basal plasma membrane and PINs is dependent on the phospholipid composition of the plasma membrane as well as on the phosphatidylinositol phosphate 5-kinases PIP5K1 and PIP5K2 in epidermis cells of the primary root. We further show that D6PK directly binds polyacidic phospholipids through a polybasic lysine-rich motif in the middle domain of the kinase. The lysine-rich motif is required for proper PIN3 phosphorylation and for auxin transport-dependent tropic growth. Polybasic motifs are also present at a conserved position in other D6PK-related kinases and required for membrane and phospholipid binding. Thus, phospholipid-dependent recruitment to membranes through polybasic motifs might not only be required for D6PK-mediated auxin transport but also other processes regulated by these, as yet, functionally uncharacterized kinases.

show abstract

“…Technical difficulties (associated with the bacterial expression of GST-PpPTENC) prevented us from assaying PTENC activity, but considering its conserved structure, similar phosphatase activity is predicted. It should be noted that PpPIPK1 and PpPIPK2 (Saavedra et al, 2009) have also been shown to have a broader substrate range when compared with mammalian (Anderson et al, 1999) or Arabidopsis counterparts (Heilmann and Heilmann, 2015). The limited specificity of PPI formation or breakdown might represent an important distinction between the PPI systems of plants and mammals (Saavedra et al, 2011).…”

Section: Ppptens Are Functionally Redundant Phosphatases Ubiquitouslymentioning

confidence: 99%

Phosphatase and tensin homolog (PTEN) is a growth repressor of both rhizoid and gametophore development in the moss Physcomitrella patens.

et al. 2015

Self Cite

View full text Add to dashboard Cite

Phosphatase and tensin homolog deleted on chromosome 10 (PTEN) is a lipid phosphatase implicated in cellular proliferation and survival. In animal cells, loss of PTEN leads to increased levels of phosphatidylinositol (3,4,5)-trisphosphate, stimulation of glucose and lipid metabolism, cellular growth, and morphological changes (related to adaptation and survival). Intriguingly, in plants, phosphatidylinositol (3,4,5)-trisphosphate has not been detected, and the enzymes that synthesize it were never reported. In this study we performed a genetic, biochemical, and functional characterization of the moss Physcomitrella patens PTEN gene family. P. patens has four PTENs, which are ubiquitously expressed during the entire moss life cycle. Using a knock-in approach, we show that all four genes are expressed in growing tissues, namely caulonemal and rhizoid cells. At the subcellular level, PpPTEN-green fluorescent protein fusions localized to the cytosol and the nucleus. Analysis of single and double knockouts revealed no significant phenotypes at different developmental stages, indicative of functional redundancy. However, compared with wild-type triple and quadruple pten knockouts, caulonemal cells grew faster, switched from the juvenile protonemal stage to adult gametophores earlier, and produced more rhizoids. Furthermore, analysis of lipid content and quantitative real-time polymerase chain reaction data performed in quadruple mutants revealed altered phosphoinositide levels [increase in phosphatidylinositol (3,5)-bisphosphate and decrease in phosphatidylinositol 3-phosphate] and up-regulation of marker genes from the synthesis phase of the cell cycle (e.g. P. patens proliferating cell nuclear antigen, ribonucleotide reductase, and minichromosome maintenance) and of the retinoblastoma-related protein gene P. patens retinoblastomarelated protein1. Together, these results suggest that PpPTEN is a suppressor of cell growth and morphogenic development in plants.

show abstract

Plant phosphoinositides—complex networks controlling growth and adaptation

Cited by 75 publications

References 130 publications

A PtdIns(4)P-driven electrostatic field controls cell membrane identity and signalling in plants

A PtdIns(4)P-driven electrostatic field controls cell membrane identity and signalling in plants

Phospholipid composition and a polybasic motif determine D6 PROTEIN KINASE polar association with the plasma membrane and tropic responses

Phosphatase and tensin homolog (PTEN) is a growth repressor of both rhizoid and gametophore development in the moss Physcomitrella patens.

Contact Info

Product

Resources

About